Softening of POPC membranes by magainin

被引：72

作者：

Bouvrais, Helene ^{[1
,2
]}

Meleard, Philippe ^{[2
]}

Pott, Tanja ^{[2
]}

Jensen, Knud J. ^{[3
]}

Brask, Jesper ^{[3
]}

Ipsen, John H. ^{[1
]}

机构：

[1] Univ So Denmark, MEMPHYS Ctr Biomembrane Phys, Dept Chem & Phys, Odense, Denmark

[2] Univ Rennes 1, CNRS, UMR 6510, Rennes, France

[3] Univ Copenhagen, Dept Nat Sci, Bioorgan Chem Sect, Frederiksberg, Denmark

来源：

BIOPHYSICAL CHEMISTRY | 2008年 / 137卷 / 01期

基金：

新加坡国家研究基金会;

关键词：

lipid bilayer; vesicle fluctuation analysis; membrane mechanics; magainin; bending elasticity; continuum model;

D O I：

10.1016/j.bpc.2008.06.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Magainin 2 belongs to the family of peptides, which interacts with the lipid membranes. The present work deals with the effect of this peptide on the mechanical properties of 1-paimitoyl-2-oleoyl-sn-glycerol-3-phosphocholine Giant Unilamellar Vesicle, characterized by the bending stiffness modulus. The ber ding elastic modulus is measured by Vesicle Fluctuation Analysis at biologically relevant pH and physiological buffer conditions and shows a dramatic decrease with increasing peptide concentration. The observed bilayer softening is interpreted in terms of a continuum model describing perturbations on the membrane organization. Our analysis suggests that the adsorbed peptides give rise to considerable local curvature disruptions of the membrane. (c) 2008 Elsevier B.V. All rights reserved.

引用

页码：7 / 12

页数：6

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